کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1185755 | 963413 | 2012 | 7 صفحه PDF | دانلود رایگان |

A 5447 Da antifungal peptide with an N-terminal sequence highly homologous to plant defensins was purified from Phaseolus vulgaris cv. ‘King Pole Bean’ by anion-exchange chromatography on Q Sepharose and FPLC-gel filtration on Superdex 75. The isolated peptide inhibited growth of a number of fungal species, including Mycosphaerella arachidicola, Saccharomyces cerevisiae and Candida albicans, with IC50 values of 3.9, 4.0 and 8.4 μM, respectively. Using the membrane non-permeable DNA-binding dye SYTOX green, it was found that the peptide increased the cell membrane permeability of M. arachidicola, S. cerevisiae and C. albicans.
► A peptide resembling plant defensins in sequence was purified from King Pole Bean.
► The peptide permeabilizes yeast cell membrane as revealed by SYTOX green staining.
► The antifungal peptide induces gene expression of tumour necrosis factor – α.
Journal: Food Chemistry - Volume 135, Issue 2, 15 November 2012, Pages 408–414